BIOMAT Database Logo BIOMAT Database Logo

Effects of 3-methylcholanthrene on oxidized nicotinamide-adenine dinucleotide phosphatedependent dehydrogenases and selected metabolites in perfused rat liver. 1980

F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
Department of Pharmacology and Experimental Therapeutics, University of Maryland School of Medicine, Baltimore, MD 21201, USA.

Treatment of adult rats with 3-methylcholanthrene over a 3-day period produced significant decreases in hepatic ATP concentrations and elevated the activities of 6-phosphogluconate dehydrogenase and malic enzyme. The decline in ATP was accompanied by a decrease in total adenine nucleotides; however, ATP/ADP ratios were essentially the same in livers of normal and 3-methylcholanthrene-treated rats, and no significant changes were noted in glycolytic and citric acid cycle intermediates. Thus, hepatic energy metabolism does not appear to be altered grossly after 3-methylcholanthrene treatment. NADP(+)/NADPH ratios calculated from substrates assumed to be in near equilibrium with malic enzyme, isocitrate dehydrogenase and 6-phosphogluconate dehydrogenase increased after 3-methylcholanthrene treatment; these changes were accompanied by significant increases in the activity of malic enzyme and 6-phosphogluconate dehydrogenase. Oxidation of hepatic NADPH and elevation of activities of several NADPH-generating enzymes by 3-methylcholanthrene indicates that this agent which induces components of the mixed-function oxidase system also elevates the capacity of the liver to form NADPH.

UI MeSH Term Description Entries
D007521 Isocitrate Dehydrogenase An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41. NAD Isocitrate Dehydrogenase,Isocitrate Dehydrogenase (NAD+),Isocitrate Dehydrogenase-I,Dehydrogenase, Isocitrate,Dehydrogenase, NAD Isocitrate,Isocitrate Dehydrogenase I,Isocitrate Dehydrogenase, NAD
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008291 Malate Dehydrogenase An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37. Malic Dehydrogenase,NAD-Malate Dehydrogenase,Dehydrogenase, Malate,Dehydrogenase, Malic,Dehydrogenase, NAD-Malate,NAD Malate Dehydrogenase
D008748 Methylcholanthrene A carcinogen that is often used in experimental cancer studies. 20-Methylcholanthrene,3-Methylcholanthrene,20 Methylcholanthrene,3 Methylcholanthrene
D009243 NAD A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D009249 NADP Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed) Coenzyme II,Nicotinamide-Adenine Dinucleotide Phosphate,Triphosphopyridine Nucleotide,NADPH,Dinucleotide Phosphate, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide Phosphate,Nucleotide, Triphosphopyridine,Phosphate, Nicotinamide-Adenine Dinucleotide
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D010477 Perfusion Treatment process involving the injection of fluid into an organ or tissue. Perfusions
D010734 Phosphogluconate Dehydrogenase An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43. 6-Phosphogluconate Dehydrogenase,6 Phosphogluconate Dehydrogenase,Dehydrogenase, 6-Phosphogluconate,Dehydrogenase, Phosphogluconate

Related Publications

F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
THE 21-HYDROXYSTEROID DEHYDROGENASES OF LIVER. A NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE AND TWO NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASES.
January 1965, The Journal of biological chemistry,
F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
OXIDIZED NICOTINAMIDE-ADENINE DINUCLEOTIDE-INDEPENDENT LACTATE DEHYDROGENASES OF LACTOBACILLUS ARABINOSUS 17.5.
September 1963, Biochimica et biophysica acta,
F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
Oxidized and reduced nicotinamide-adenine dinucleotide phosphate in tissue suspensions of rat liver.
September 1967, The Biochemical journal,
F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
Inhibition of rat liver nicotinamide adenine dinucleotide kinase by reduced nicotinamide adenine dinucleotide phosphate.
February 1968, The Journal of biological chemistry,
F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
Nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate-linked succinic semialdehyde dehydrogenases in a Pseudonomas species.
October 1969, Journal of bacteriology,
F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
The effect of ethionine on the synthesis of nicotinamide-adenine dinucleotide and nicotinamide-adenine dinucleotide phosphate in rat liver.
November 1964, The Biochemical journal,
F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
The oxidized form of nicotinamide adenine dinucleotide.
June 2000, Acta crystallographica. Section C, Crystal structure communications,
F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
L-Glycerol 3-phosphate dehydrogenases. II. Effects of phosphorylated compounds on nicotinamide adenine dinucleotide linked enzyme from rabbit liver.
August 1973, The Journal of biological chemistry,
F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
Regulation of the nicotinamide adenine dinucleotide- and nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenases of Saccharomyces cerevisiae.
October 1973, Journal of bacteriology,
F C Kauffman, and R K Evans, and L A Reinke, and S A Belinsky, and C Ballow, and R G Thurman
pH-dependent inactivation of nicotinamide--adenine dinucleotide glycohydrolase by its substrate, oxidized nicotinamide--adenine dinucleotide.
June 1971, Biochemistry,
Copied contents to your clipboard!